ID   SYV_PROMM               Reviewed;         929 AA.
AC   Q7TUI9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=PMT_2191;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE22365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX548175; CAE22365.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7TUI9; -.
DR   SMR; Q7TUI9; -.
DR   STRING; 74547.PMT_2191; -.
DR   PRIDE; Q7TUI9; -.
DR   EnsemblBacteria; CAE22365; CAE22365; PMT_2191.
DR   KEGG; pmt:PMT_2191; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_3; -.
DR   Proteomes; UP000001423; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..929
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224531"
FT   COILED          862..929
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           59..69
FT                   /note="'HIGH' region"
FT   MOTIF           557..561
FT                   /note="'KMSKS' region"
FT   BINDING         560
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   929 AA;  103444 MW;  F6123CD7BED721AC CRC64;
     MTELSAADPA FVQAADALAK TYDPAGTESR WQCAWEESGV FHPDPQAAGE PFSVVIPPPN
     VTGSLHMGHA FNTALIDTIV RFQRLQGKNV LCLPGTDHAS IAVQTILEKQ LKAEAISRYD
     LGREAFLERA WAWKEESGGR IVDQLRRLGY SVDWQRQRFT LDEGLSAAVR EAFVRLHEQG
     LIYRGEYLVN WCPASGSAVS DLEVEMKEVD GHLWHLRYPL TGGPAADGTT HLEVATTRPE
     TMLGDVAVAV NPADERYRHL VGQTLILPLL GREIPVIADD HVDQDFGTGC VKVTPAHDPN
     DFAIGRRHDL PQITVMNKNG SMNGHAGRFE GLDRFEARKA VVAALQEEGL LVKVEPHRHS
     VPYSDRGKVP VEPLLSTQWF VRMEPLAARC HECLDHGAPR FVPNRWQKVY RDWLTEIRDW
     CISRQLWWGH RIPAWFVVSE TDDQLTDATP YLVARSEEEA WQQARDQFGE AVVIQQDEDV
     LDTWFSSGLW PFSTMGWPDQ ESADLECWYP TSTLVTGFDI IFFWVARMTM MAGAFTGRMP
     FADVYIHGLV RDEQNRKMSK SAGNGIDPLL LIERYGTDAL RFALVREVAG AGQDIRLDYD
     RKSDTSATVE AARNFANKLW NATRFALMNL GGETPASLGE PDPASLQLAD RWILSRLARM
     NRDVVERYDS YRLGEAAKCL YEFAWNDICD WYLELSKRRL HPGEDASGEV LADQCTARQV
     LAKVLADLLV MLHPLMPHLS EELWHGLTGA PKDTFLALQS WPASNKSFLD DALELSFTEL
     IEAIRVVRNL RAVAGLKPAQ TVPVQFITGR PELAALLEQA TADITALTRA ESVVVATSAD
     LTQRCLAGVS GELQVLLPID GLVDLDALRG RLEKDLAKAE KEIAGLAGRL ANPNFAIKAP
     PNVVEECQSN LAEAEAQAEL ARQRLSDLG